Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex

Corey F. Hryc, Venkata K. P. S. Mallampalli, Evgeniy I. Bovshik, Stavros Azinas, Guizhen Fan, Irina I. Serysheva, Genevieve C. Sparagna, Matthew L. Baker (), Eugenia Mileykovskaya () and William Dowhan ()
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Corey F. Hryc: McGovern Medical School at the University of Texas Health Science Center
Venkata K. P. S. Mallampalli: McGovern Medical School at the University of Texas Health Science Center
Evgeniy I. Bovshik: McGovern Medical School at the University of Texas Health Science Center
Stavros Azinas: McGovern Medical School at the University of Texas Health Science Center
Guizhen Fan: McGovern Medical School at the University of Texas Health Science Center
Irina I. Serysheva: McGovern Medical School at the University of Texas Health Science Center
Genevieve C. Sparagna: University of Colorado Anschutz Medical Campus
Matthew L. Baker: McGovern Medical School at the University of Texas Health Science Center
Eugenia Mileykovskaya: McGovern Medical School at the University of Texas Health Science Center
William Dowhan: McGovern Medical School at the University of Texas Health Science Center

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: Abstract Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IV1III2IV1) and a supercomplex (III2IV1) isolated from a cardiolipin-lacking Saccharomyces cerevisiae mutant at 3.2-Å and 3.3-Å resolution, respectively, and demonstrate that phosphatidylglycerol in III2IV1 occupies similar positions as cardiolipin in IV1III2IV1. Lipid-protein interactions within these complexes differ, which conceivably underlies the reduced level of IV1III2IV1 and high levels of III2IV1 and free III2 and IV in mutant mitochondria. Here we show that anionic phospholipids interact with positive amino acids and appear to nucleate a phospholipid domain at the interface between the individual complexes, which dampen charge repulsion and further stabilize interaction, respectively, between individual complexes.

Date: 2023
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DOI: 10.1038/s41467-023-38441-5

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